Related ArticlesNMR study on the interaction between MHC class I protein and its antigen peptide.
Biochem Biophys Res Commun. 2000 Nov 30;278(3):609-13
Authors: Nakagawa M, Chiba-Kamoshida K, Udaka K, Nakanishi H
A major histcompatibility complex (MHC) class I protein H-2K(b) was expressed in a large scale as a fusion protein with thioredoxin and hexahistidine at the N-terminus to analyze the interaction with the antigen peptide SIYRYYGL. NMR spectra of the peptide in the mixture solution with the protein showed very broad signals, indicating the obviously clear existence of the dynamic interaction between the class I protein and the antigen peptide. The interaction of the protein and peptide was discussed as well as the surrounding atmosphere of the peptide in the complex.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Structure and lipid interactions of an anti-inflammatory and anti-atherogenic 10-residue class G(*) apolipoprotein J peptide using solution NMR.
Biochim Biophys Acta. 2011 Jan;1808(1):498-507
Authors: Mishra VK, Palgunachari MN, Hudson JS, Shin R, Keenum TD, Krishna NR, Anantharamaiah GM
The surprising observation that a 10-residue class G(?) peptide from apolipoprotein J, apoJ, possesses...
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[Question from NMRWiki Q&A forum] peptide protein interaction
peptide protein interaction
I have determined the structure of a 110 residues protein(11kDa) which is known to interact with a 15mer peptide. Now I am interested to know which residues of the 15mer peptide interacts with this 11kDa protein. Can anyone suggest a simple nmr experiment which can tell the residues from the 15mer peptide which interact with the protein.
Check if somebody has answered this question on NMRWiki QA forum
[NMR paper] Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes st
Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Related Articles Interaction of the fusogenic peptide B18 in its amyloid-state with lipid membranes studied by solid state NMR.
Chem Phys Lipids. 2004 Nov;132(1):65-77
Authors: Grage SL, Afonin S, Grüne M, Ulrich AS
The interaction of the fusogenic polypeptide segment "B18" from the fertilization protein binding with lipid membranes was investigated by solid state 2H and 31P NMR, and by differential scanning calorimetry. B18 is known...
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11-24-2010 10:03 PM
[NMR paper] The cisproline(i - 1)-aromatic(i) interaction: folding of the Ala-cisPro-Tyr peptide
The cisproline(i - 1)-aromatic(i) interaction: folding of the Ala-cisPro-Tyr peptide characterized by NMR and theoretical approaches.
Related Articles The cisproline(i - 1)-aromatic(i) interaction: folding of the Ala-cisPro-Tyr peptide characterized by NMR and theoretical approaches.
J Biomol NMR. 2000 May;17(1):63-77
Authors: Nardi F, Kemmink J, Sattler M, Wade RC
Cisproline(i - 1)-aromatic(i) interactions have been detected in several short peptides in aqueous solution by analysis of anomalous chemical shifts measured by 1H-NMR spectroscopy....
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11-18-2010 09:15 PM
[NMR paper] NMR diffusion and relaxation study of drug-protein interaction.
NMR diffusion and relaxation study of drug-protein interaction.
Related Articles NMR diffusion and relaxation study of drug-protein interaction.
Spectrochim Acta A Mol Biomol Spectrosc. 1999 Aug;55A(9):1897-901
Authors: Luo RS, Liu ML, Mao XA
In this work, NMR diffusion and relaxation measurements are applied to the study of the interaction between the anti-inflammatory drug salicylate and the human serum albumin (HSA) in solutions. The self-diffusion coefficients and the spin-lattice relaxation rates of salicylate are measured as a function...
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[NMR paper] NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
Related Articles NMR identification of epitopes of Lyme disease antigen OspA to monoclonal antibodies.
J Mol Biol. 1998 Aug 7;281(1):61-7
Authors: Huang X, Yang X, Luft BJ, Koide S
Outer surface protein A (OspA) from the Lyme disease spirochete Borrelia burgdorferi has been a focus of vaccine development. We have identified epitopes of OspA to two monoclonal antibodies (mAbs) by comparing NMR chemical shifts of free OspA and those in Fab complexes....
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11-17-2010 11:15 PM
[NMR paper] NMR study of the interaction between the B domain of staphylococcal protein A and the
NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.
Related Articles NMR study of the interaction between the B domain of staphylococcal protein A and the Fc portion of immunoglobulin G.
Biochemistry. 1998 Jan 6;37(1):129-36
Authors: Gouda H, Shiraishi M, Takahashi H, Kato K, Torigoe H, Arata Y, Shimada I
The solution structure of the B domain of staphylococcal protein A (FB) complexed with the Fc fragment of immunoglobulin G (IgG) is reported. A previous NMR analysis has shown...
NMR study on the interaction between MHC class I protein and its antigen peptide.
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